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Heavy atoms in protein crystals significantly increase radiation damage during serial femtosecond X-ray crystallography (SFX) experiments. Understanding this electronic damage is crucial for improving X-ray free-electron laser (XFEL) structural studies.

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Area of Science:

  • Structural biology
  • Biophysics
  • Materials science

Background:

  • Serial femtosecond X-ray crystallography (SFX) uses X-ray free-electron lasers (XFELs) to determine biomolecular structures.
  • XFEL pulses outrun conventional radiation damage but are limited by rapid electronic damage from ionization.
  • Understanding ionization dynamics is key to mitigating damage in XFEL crystallography.

Purpose of the Study:

  • To differentiate the impact of various atomic species on protein crystal ionization.
  • To quantify the contribution of heavy atoms to radiation damage in SFX.
  • To identify optimal X-ray energies for minimizing ionization cascades.

Main Methods:

  • Utilized a plasma code to simulate electron energy distributions and track ionization.
  • Modeled ionization cascades initiated by photoelectrons from different atomic species.
  • Analyzed the effect of heavy atoms (Z > 10), sulfur, and solvated salts on light-atom ionization.

Main Results:

  • Trace amounts of heavy atoms (Z > 10) significantly seed electron ionization cascades, contributing substantially to global radiation damage.
  • Sulfur atoms and solvated salts in protein crystals induce considerable light-atom ionization.
  • Global ionization peaks at approximately 2 keV above inner-shell absorption edges, initiating brief ionization cascades.

Conclusions:

  • Heavy elements, even in small quantities, critically influence radiation damage in XFEL experiments.
  • Minimizing heavy atom content or selecting appropriate X-ray energies can reduce damage.
  • This research provides insights for optimizing experimental parameters in XFEL crystallography.